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Journal Article
Analytical and Bioanalytical Chemistry, ISSN 1618-2642, 10/2017, Volume 409, Issue 25, pp. 6015 - 6026
We developed a simple analytical method for the simultaneous determination of representatives of various groups of neurotoxic insecticides (carbaryl,... 
Biochemistry, general | Chemistry | Analytical Chemistry | Mini-extractor | Food Science | Monitoring/Environmental Analysis | Animal tissues | Tissue extract clean-up | Characterization and Evaluation of Materials | Insecticides | Laboratory Medicine | Neurodevelopmental toxicity | CHEMISTRY, ANALYTICAL | BIOCHEMICAL RESEARCH METHODS | MASS-SPECTROMETRY | PESTICIDES | Chromatography, Gel - methods | Gas Chromatography-Mass Spectrometry - methods | Limit of Detection | Solid Phase Extraction - instrumentation | Sonication - instrumentation | Rats | Insecticides - isolation & purification | Chromatography, Gel - instrumentation | Neurotoxins - analysis | Equipment Design | Liver - chemistry | Neurotoxins - isolation & purification | Sonication - methods | Animals | Neurotoxins - pharmacokinetics | Solid Phase Extraction - methods | Female | Adipose Tissue - chemistry | Brain Chemistry | Insecticides - analysis | Insecticides - pharmacokinetics | Extraction (Chemistry) | Lipids | Chemical properties | Health aspects | Methods | Neurotoxic agents | Endosulfan | Brain | High resolution | Aluminum | Liver | Sulfates | Silica | Silicon dioxide | Neurotoxicity | Agrochemicals | Cypermethrin | Sodium sulfate | Extraction | Chlorpyrifos | Pesticides | Mass spectroscopy | Liquid chromatography | Chromatography | Aluminum oxide | Gas chromatography | Extractors | Sodium | Carbaryl | Sulfate | Mass spectrometry
Journal Article
Kidney International, ISSN 0085-2538, 07/2014, Volume 86, Issue 1, pp. 75 - 85
Fibrosis is a hallmark of chronic kidney disease, for which there is currently no effective cure. The hormone relaxin is emerging as an effective antifibrotic... 
Smad2 | kidney disease | TGF-β | fibrosis | relaxin | AT2 receptor | KIDNEY-DISEASE | NITRIC-OXIDE SYNTHASE | PROTEIN-KINASE | RESONANCE ENERGY-TRANSFER | FIBROBLASTS | TGF-beta | GROWTH-FACTOR-BETA | AT RECEPTORS | IN-VIVO | UROLOGY & NEPHROLOGY | HYPERTENSIVE-RATS | HORMONE RELAXIN | Relaxin - metabolism | Kidney - pathology | Receptors, G-Protein-Coupled - metabolism | Transforming Growth Factor beta1 - antagonists & inhibitors | Humans | Protein Multimerization | Male | Receptors, Peptide - chemistry | Angiotensin II Type 2 Receptor Blockers - pharmacology | Relaxin - pharmacology | Renal Insufficiency, Chronic - drug therapy | Myofibroblasts - metabolism | Renal Insufficiency, Chronic - metabolism | Kidney - metabolism | Myofibroblasts - pathology | Receptor, Angiotensin, Type 2 - genetics | Kidney - drug effects | Cells, Cultured | Rats | Imidazoles - pharmacology | Recombinant Proteins - pharmacology | Myofibroblasts - drug effects | Rats, Sprague-Dawley | Disease Progression | Mice, Knockout | Renal Insufficiency, Chronic - pathology | Animals | MAP Kinase Signaling System - drug effects | Receptor, Angiotensin, Type 2 - metabolism | Signal Transduction - drug effects | Fibrosis | Mice | Pyridines - pharmacology | Receptor, Angiotensin, Type 2 - deficiency | Receptors, G-Protein-Coupled - chemistry | Receptors, Peptide - metabolism
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2018, Volume 13, Issue 8, p. e0202408
Toll like receptors (TLRs) are important pattern recognition receptors that can detect pathogen and danger associated molecular patterns to initiate an innate... 
SIGNAL-TRANSDUCTION | TRANSFER BRET | ACTIVATION | PATHWAY | MULTIDISCIPLINARY SCIENCES | TOLL-LIKE RECEPTORS | INDUCTION | IDENTIFICATION | ADAPTER PROTEIN | BINDING | FAMILY | Gene Expression | Toll-Like Receptor 2 - genetics | Membrane Glycoproteins - metabolism | Lipopeptides - pharmacology | Humans | Receptors, Interleukin-1 - genetics | Myeloid Differentiation Factor 88 - genetics | Signal Transduction - genetics | Toll-Like Receptor 2 - metabolism | Membrane Glycoproteins - genetics | Receptors, Interleukin-1 - metabolism | Microscopy, Confocal | Signal Transduction - drug effects | HEK293 Cells | Fluorescence Resonance Energy Transfer | Myeloid Differentiation Factor 88 - metabolism | Cytokines | Gene expression | Research | Bioluminescence | Transcription factors | Immunoprecipitation | Confocal microscopy | Biology | Activation | Kinases | Recruitment | Proteins | Signal transduction | Receptors | Immunology | Transcription activation | Toll-like receptors | Artefacts | Immune system | Binding | Adaptor proteins | CRISPR | Medical research | NF-κB protein | Immune response | Cell walls | Hazards | Pattern recognition | Adaptors | Real time | Artifacts | TLR1 protein | Microscopy | TLR2 protein | Tagging | MyD88 protein | Ligands | Resonance | Dimers | Kinetics | Receptor mechanisms | Protein interaction | Lipopeptides | Energy transfer
Journal Article
British Journal of Pharmacology, ISSN 0007-1188, 05/2017, Volume 174, Issue 10, pp. 1077 - 1089
Background and Purpose Insulin‐like peptide 5 (INSL5) is a two‐chain, three‐disulfide‐bonded peptide of the insulin/relaxin superfamily, uniquely expressed in... 
GLUCOSE-HOMEOSTASIS | NEUROENDOCRINE TUMORS | S6 PHOSPHORYLATION | CONCISE GUIDE | BETA-ARRESTINS | PROTEIN-COUPLED RECEPTORS | CELL-SIZE | PHARMACOLOGY & PHARMACY | IDENTIFICATION | INSL5 | C-SRC | Insulin - pharmacology | Phosphorylation | Cricetulus | Receptors, G-Protein-Coupled - metabolism | Humans | Cells, Cultured | Structure-Activity Relationship | Extracellular Signal-Regulated MAP Kinases - metabolism | Dose-Response Relationship, Drug | Cyclic AMP - antagonists & inhibitors | Animals | Signal Transduction - drug effects | Ribosomal Protein S6 - metabolism | Cell Proliferation - drug effects | Mice | Proteins - pharmacology | p38 Mitogen-Activated Protein Kinases - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Cyclic AMP - metabolism | CHO Cells | Receptors, Peptide - metabolism | Cell proliferation | G protein-coupled receptors | Peptides | b-Adrenergic-receptor kinase | Insulinoma | Bromodeoxyuridine | Nervous system | AKT protein | Kinases | Pertussis toxin | Accumulation | K-Ras protein | Recruitment | Proteins | Pertussis | Signal transduction | Receptors | Enteric nervous system | Transfection | Pathways | Colon | Inhibition | Calcium (intracellular) | Secretion | Extracellular signal-regulated kinase | Cyclic AMP | Gene expression | Real time | Insulin | Relaxin | Mutants | Signaling | Forskolin | Transduction | Receptor mechanisms | Themed Section | Research Paper
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 2968 - 14
Journal Article
Pharmacology and Therapeutics, ISSN 0163-7258, 07/2018, Volume 187, pp. 114 - 132
The peptide relaxin was first identified as an important circulating hormone during pregnancy over 90 years ago. Research over many years defined the numerous... 
GPCR | insulin-like peptides | Relaxin | RXFP1 | LGR | Evolution | G proteins | Peptides | Health aspects
Journal Article
Naunyn-Schmiedeberg's Archives of Pharmacology, ISSN 0028-1298, 1/2017, Volume 390, Issue 1, pp. 105 - 111
The relaxin family peptide receptor 4 (RXFP4) is a G protein-coupled receptor (GPCR) expressed in the colorectum with emerging roles in metabolism and appetite... 
Signal transduction | Neurosciences | Biomedicine | Insulin-like peptide 5 | Insulin-like peptide 3 | Pharmacology/Toxicology | Relaxin family peptide receptor 4 | Relaxin-3 | Relaxin-2 | ELECTROSTATIC INTERACTIONS | NEUROENDOCRINE TUMORS | GPCR142 | H2 RELAXIN | IDENTIFICATION | IN-VITRO | PHARMACOLOGY & PHARMACY | H3 RELAXIN | LIGAND | BINDING | INSL5 | Phosphorylation | Cricetulus | Receptors, G-Protein-Coupled - metabolism | Ribosomal Protein S6 Kinases - metabolism | Receptors, Peptide - agonists | Humans | beta-Arrestins - metabolism | Extracellular Signal-Regulated MAP Kinases - metabolism | G-Protein-Coupled Receptor Kinase 2 - metabolism | Receptors, G-Protein-Coupled - agonists | Receptors, Peptide - genetics | Relaxin - pharmacology | Dose-Response Relationship, Drug | Transfection | Time Factors | p38 Mitogen-Activated Protein Kinases - metabolism | Proto-Oncogene Proteins c-akt - metabolism | CHO Cells | Insulin - pharmacology | Adenylyl Cyclases - metabolism | Protein Transport | Animals | Signal Transduction - drug effects | Ligands | Cell Proliferation - drug effects | Proteins - pharmacology | Receptors, G-Protein-Coupled - genetics | Enzyme Activation | Receptors, Peptide - metabolism | Peptides | Resveratrol | Physiological aspects | Cellular signal transduction | Drug discovery | G proteins | Molecular biology | Insulin | Membrane proteins
Journal Article
Methods in molecular biology (Clifton, N.J.), ISSN 1064-3745, 2009, Volume 552, pp. 305 - 317
Bioluminescence resonance energy transfer (BRET) is a powerful and increasingly popular technique for studying protein-protein interactions in live cells and... 
Luciferases - metabolism | Receptors, G-Protein-Coupled - metabolism | beta-Arrestins | Humans | Energy Transfer | Arrestins - metabolism | Luminescent Measurements - methods
Journal Article